Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways
Direct visualization of pathways followed by single molecules while they spontaneously self-assemble into supramolecular biological machines may provide fundamental knowledge to guide molecular therapeutics and the bottom-up design of nanomaterials and nanodevices. Here, high-speed atomic force micr...
| Autores: | , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2020 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/241852 |
| Acceso en línea: | http://hdl.handle.net/10261/241852 |
| Access Level: | acceso abierto |
| Palabra clave: | Self-assembly Nanomaterials Virus Capsid proteins Single-molecule High-speed atomic force microscopy |
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Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic PathwaysValbuena, AlejandroMaity, SouravMateu, Mauricio G.Roos, Wouter H.Self-assemblyNanomaterialsVirusCapsid proteinsSingle-moleculeHigh-speed atomic force microscopyDirect visualization of pathways followed by single molecules while they spontaneously self-assemble into supramolecular biological machines may provide fundamental knowledge to guide molecular therapeutics and the bottom-up design of nanomaterials and nanodevices. Here, high-speed atomic force microscopy is used to visualize self-assembly of the bidimensional lattice of protein molecules that constitutes the framework of the mature human immunodeficiency virus capsid. By real-time imaging of the assembly reaction, individual transient intermediates and reaction pathways followed by single molecules could be revealed. As when assembling a jigsaw puzzle, the capsid protein lattice is randomly built. Lattice patches grow independently from separate nucleation events whereby individual molecules follow different paths. Protein subunits can be added individually, while others form oligomers before joining a lattice or are occasionally removed from the latter. Direct real-time imaging of supramolecular self-assembly has revealed a complex, chaotic process involving multiple routes followed by individual molecules that are inaccessible to bulk (averaging) techniques.MICINN/FEDER EU (Spain, BIO2015-69928-R and RTI2018-096635-B-100) to M.G.M. and a VIDI grant from the Nederlandse Organisatie voor Wetenschappelijk Onderzoek and a STW-Perspectief grant “Cancer-ID” to W.H.R. A travel grant to A.V. by the European ARBRE-Mobieu ConsortiumAmerican Chemical SocietyMinisterio de Ciencia e Innovación (España)Netherlands Organization for Scientific ResearchConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2021202120202021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/241852reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1021/acsnano.0c03207Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2418522026-05-22T06:33:51Z |
| dc.title.none.fl_str_mv |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways |
| title |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways |
| spellingShingle |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways Valbuena, Alejandro Self-assembly Nanomaterials Virus Capsid proteins Single-molecule High-speed atomic force microscopy |
| title_short |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways |
| title_full |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways |
| title_fullStr |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways |
| title_full_unstemmed |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways |
| title_sort |
Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways |
| dc.creator.none.fl_str_mv |
Valbuena, Alejandro Maity, Sourav Mateu, Mauricio G. Roos, Wouter H. |
| author |
Valbuena, Alejandro |
| author_facet |
Valbuena, Alejandro Maity, Sourav Mateu, Mauricio G. Roos, Wouter H. |
| author_role |
author |
| author2 |
Maity, Sourav Mateu, Mauricio G. Roos, Wouter H. |
| author2_role |
author author author |
| dc.contributor.none.fl_str_mv |
Ministerio de Ciencia e Innovación (España) Netherlands Organization for Scientific Research Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] |
| dc.subject.none.fl_str_mv |
Self-assembly Nanomaterials Virus Capsid proteins Single-molecule High-speed atomic force microscopy |
| topic |
Self-assembly Nanomaterials Virus Capsid proteins Single-molecule High-speed atomic force microscopy |
| description |
Direct visualization of pathways followed by single molecules while they spontaneously self-assemble into supramolecular biological machines may provide fundamental knowledge to guide molecular therapeutics and the bottom-up design of nanomaterials and nanodevices. Here, high-speed atomic force microscopy is used to visualize self-assembly of the bidimensional lattice of protein molecules that constitutes the framework of the mature human immunodeficiency virus capsid. By real-time imaging of the assembly reaction, individual transient intermediates and reaction pathways followed by single molecules could be revealed. As when assembling a jigsaw puzzle, the capsid protein lattice is randomly built. Lattice patches grow independently from separate nucleation events whereby individual molecules follow different paths. Protein subunits can be added individually, while others form oligomers before joining a lattice or are occasionally removed from the latter. Direct real-time imaging of supramolecular self-assembly has revealed a complex, chaotic process involving multiple routes followed by individual molecules that are inaccessible to bulk (averaging) techniques. |
| publishDate |
2020 |
| dc.date.none.fl_str_mv |
2020 2021 2021 2021 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article http://purl.org/coar/resource_type/c_6501 Publisher's version info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
http://hdl.handle.net/10261/241852 |
| url |
http://hdl.handle.net/10261/241852 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
http://dx.doi.org/10.1021/acsnano.0c03207 Sí |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.publisher.none.fl_str_mv |
American Chemical Society |
| publisher.none.fl_str_mv |
American Chemical Society |
| dc.source.none.fl_str_mv |
reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC instname:Consejo Superior de Investigaciones Científicas (CSIC) |
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Consejo Superior de Investigaciones Científicas (CSIC) |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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DIGITAL.CSIC. Repositorio Institucional del CSIC |
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1869403658980950016 |
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15.811543 |